ABSTRACT
This paper describes the development of unobtrusive room sensors to discover relationships between sleep quality and the clinical assessments of combat soldiers suffering from post-traumatic stress disorder (PTSD) and mild traumatic brain injury (TBI). We consider the use of a remote room sensor unit composed of a Doppler radar, light, sound and other room environment sensors. We also employ an actigraphy watch. We discuss sensor implementation, radar data analytics and preliminary results using real data from a Warrior Transition Battalion located in Fort Gordon, GA. Two radar analytical approaches are developed and compared against the actigraphy watch estimates--one, emphasizing system knowledge; and the other, clustering on several radar signal features. The radar analytic algorithms are able to estimate sleep periods, signal absence and restlessness in the bed. In our test cases, the radar estimates are shown to agree with the actigraphy watch. PTSD and mild-TBI soldiers do often show signs of sporadic and restless sleep. Ongoing research results are expected to provide further insight.
Subject(s)
Actigraphy/methods , Brain Injuries/diagnosis , Military Personnel , Monitoring, Ambulatory/methods , Polysomnography/methods , Sleep Stages , Stress Disorders, Post-Traumatic/diagnosis , Adult , Humans , Male , Middle Aged , Point-of-Care Systems , Radar , Reproducibility of Results , Sensitivity and Specificity , Stress Disorders, Post-Traumatic/physiopathology , Young AdultABSTRACT
BACKGROUND: We have recently shown that S-nitrosothiols (RSNOs) decompose in aqueous buffer to give nitric oxide, an important signalling molecule, and the corresponding disulphides. This occurs by reaction with Cu+ generated from Cu2+ (supplied as hydrated Cu2+) by thiolate reduction. To establish whether these reactions are feasible in vivo, we set out to determine whether Cu2+ bound to an amino acid, a tripeptide or to human serum albumin (HSA) could serve as a Cu+ source for generation of NO from S-nitrosothiols. RESULTS: Experiments with Cu2+ bound to the tripeptide Gly-Gly-His or to two histidine molecules or to HSA showed that Cu+ was released (and trapped with neocuproine) when the copper source was treated with a thiol at pH 7.4. RSNO decomposition was achieved with all three copper sources, although not as rapidly as with added hydrated Cu2+. Decomposition was also catalyzed by ceruloplasmin. CONCLUSIONS: These results show clearly that amino-acid- and protein-bound Cu2+ can be reduced by thiolate ion to Cu+, which will generate NO from RSNO species, thus providing a realistic model for these reactions in vivo.
